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α-Smooth muscle actin expression in stroma of basal cell epithelioma (BCE)
INTOLERANCETO EXTERNALSTIM”L1. ESPECIALLY SHAMPOOSIN PATIENTS WITH ?.TOPlC DERMATITlS
SKIN CONTACT REACTION WITH OVALBUMIN IN NEW BORN GUINEA PIGS FROM SENSITIZED MATERNAL ANIMALS, ABDUL MANNAN BHUTTO, KEISUKE MAEDA, SADAO AND HIKOTARO YOSHIDA. Department of Dermatology, saki University School of Medicine, Nagasaki, Japan.
ANAN NagaOsaka
To elucidate the role of ovalbumln (OA) in pathogen&s of atoplc dermatitis, new born guinea pigs sensitized with OA I” utero were patch tested. Four groups (A, 8, C and Dj of mid term pregnant gumea pigs consisting of five animals were provided for this study. Group A; immunized by intradermal injection of OA in CFA, group B, immunized by oral administration of 1% OA in drinking water, grow C: immunized bv both methods. and erouo D: not immumzed. The &w b&n &&a pigs of each group were patch tested with 10% OA in white petrclatum. The positive reaction was seen only in the baby animals born in roup C. Histologically, the reaction site revealed remarkable in F:lltratmn of lymphocytes, eosinophlls, basophils and mast cells. By immunoiluorescence study, OA antigens were detected both in the dermis and epidermis. But, there was no OA antigen in negative reactlo” site of patch testing with OA. From these fmdings, it may conclude that OA antigen can sensitize fetus ammal. The sensitized animal can show positive reaction of patch testinz with OA.
It
1s well
known that
most patients
wrth
atopic
dermatitis
are less tolerable to the diverse external stimuli, such as however, recent interests of dennatolosoaps and shampoos. gist* seem to go to the mvolvement of allergic reactions with atoplc dermatitis. Thus, the association of atopic dermatltis with chronic irritant contact dermatitis are often rnssed or disregarded. In addition, the latest trend to shampoo everyday among youngsters leads to increase the mmher of patients with shampoo dermatitis. and to aggravate the A trml to use a hypoisritant symptoms of atopic dermatitis. shampoo was made in 28 patxnts with atopic dermatitis. Four weeks after daily applications of the product, the final global xqxovement. rating was 53.6% (15/28) in patients who FL-an the results obshowed better than slight improvement. it is presumed that approximately half of atopic patamed, tients are associated with irritant contact dermatitis from common shampoo products
El5 SPECIFIC BINDING OF TMH MONOCLONAL ANTIBODIES TO THE b-LOCUS PKOTEIN, NOT TO THE AUTHENTIC TYROSINASE ENCODED AT THE c-LOCUS. Y. TOMITA, J. MATSUNAGA. & H. TAGAMI. Department of Dermatolwv. Tohoku Umversitv School of Medicme. Sendai TMH hybridomas were previously reported by Tomita et al. to produce monoclonal antibodies against murine and human T4tyrosinase (J Invest Dermatol 85:4X. 1985). However, TMH antibodies were unable to react with K1735 cells transfected with the authentic tyrosinase-cDNA construct but did react with those transfected with the pMT4-cDNA construct. The cDNA pMT4 was initially cloned as a putative tyrosinase cDNA by Shibahara et al. (Nucl Acld Res 14:2413, 1986), but it is now known to encode mouse brown (b) locus protein named “tyrosinase-related protein” by Jackson. TMH antibodies also recogmze hair bulbs of C~~BL/~J-@‘J/C?J mouse (B/B, c/c) lacking tyrosinase activity. but do not recoanize hair bulbs of b-locus DBAL? mutated m&se these
(b/b, c/C) observatmns,
recognize
which have authentic we conclude that
the protein
encoded
tyrosmase.
Considering
TMH antibodies at b-locus.
specifically
El8
El7 Subcellular Distribution Of Catechol-0.Methyltransferase And Melanotic Malignant Melanoma TAKAKAZU MISHIMA.
a-SMOOTH MUSCLE ACTIN EXPRESSION CELL EPI’IUELIOMA (BCE)
In Amelanotic
IN STROMA OF BASAL
TSUKAMOTO, WTAKA MWLlMA Department of Dermatology, Kobe University School of Medicine, Kobc, Japan
HIDEKAZU
SHIBATA, STAN PAVEL,MASAMITSU ICHIHASHI ANDYUTAKA Department of Dermatology, Kobe Univ. School of Medicine, Kobe
During melanogenes~s, not all indolic and phsnollc compounds incorporate 1nt0 the melanin polymer. Molecuiss which escape from their place of origin due to their easy oxidability to reactive quinones. may represent a threat to pigment cells O-methvlation catalvzed bv catechol.0.methvltransferase(COMT) prwents this oxidation and polymenratlon. Thus COMT is thought a protective mechanism in melanccytes and may even play a pan in the control of melanin formation. We studied subcellular localization of COMT in transplanted melanotic and amelanotlc hamster melanoma. Results show that COMT appears to be a cytoplasmic enzyme partly integrated with microsomes. Subcellular fractions obtained from ametanotic melanoma have been found to possess higher COMT activity than those from the pigmented tumor. The relatively low spwfic activity of COMT in coated vesicle fractions does not support 10sinhibitory function m melanin polymerization within these structures. However, COMT piefeient~atly located in cytosol and cytosolic membrane network cwtd save a detoxification role I” melanocytes.
is a major component of cytoskeletal proteins. B- and y- actin are expressed in all eukaryotic cells. We previously examined the altered expression of a-smooth muscle actin (a-Sm) in human pigment cell tumors by immunohistochemical analysis using anti-a-Sm monoclonal antibody (MoAb). This revealed a uniquely intense expression of a-&n in stroma surrounding melanoma cell nests, which was not seen in benign pigment cell tumors such as nexus cell nest. In this study, we examined immunohistochemically the expression of a-Sm in BCE which was often involved in desmoplastic response. At high frequency, anti-c&n MoAb positive myoiibroblasts were detected in desmoplasia surrounding BCE nests. Additionally, some tumor cells within a few cases showed anti-&m MoAb positive staining. It is suggested that desmoplasia in BCE might be caused by paracrine secretion of tumor cells. Actin usually
,
228
SKIN CONTACT REACTION WITH OVALBUMIN IN NEW BORN GUINEA PIGS FROM SENSITIZED MATERNAL ANIMALS, ABDUL MANNAN BHUTTO, KEISUKE MAEDA, SADAO AND HIKOTARO YOSHIDA. Department of Dermatology, saki University School of Medicine, Nagasaki, Japan.
ANAN NagaOsaka
To elucidate the role of ovalbumln (OA) in pathogen&s of atoplc dermatitis, new born guinea pigs sensitized with OA I” utero were patch tested. Four groups (A, 8, C and Dj of mid term pregnant gumea pigs consisting of five animals were provided for this study. Group A; immunized by intradermal injection of OA in CFA, group B, immunized by oral administration of 1% OA in drinking water, grow C: immunized bv both methods. and erouo D: not immumzed. The &w b&n &&a pigs of each group were patch tested with 10% OA in white petrclatum. The positive reaction was seen only in the baby animals born in roup C. Histologically, the reaction site revealed remarkable in F:lltratmn of lymphocytes, eosinophlls, basophils and mast cells. By immunoiluorescence study, OA antigens were detected both in the dermis and epidermis. But, there was no OA antigen in negative reactlo” site of patch testing with OA. From these fmdings, it may conclude that OA antigen can sensitize fetus ammal. The sensitized animal can show positive reaction of patch testinz with OA.
It
1s well
known that
most patients
wrth
atopic
dermatitis
are less tolerable to the diverse external stimuli, such as however, recent interests of dennatolosoaps and shampoos. gist* seem to go to the mvolvement of allergic reactions with atoplc dermatitis. Thus, the association of atopic dermatltis with chronic irritant contact dermatitis are often rnssed or disregarded. In addition, the latest trend to shampoo everyday among youngsters leads to increase the mmher of patients with shampoo dermatitis. and to aggravate the A trml to use a hypoisritant symptoms of atopic dermatitis. shampoo was made in 28 patxnts with atopic dermatitis. Four weeks after daily applications of the product, the final global xqxovement. rating was 53.6% (15/28) in patients who FL-an the results obshowed better than slight improvement. it is presumed that approximately half of atopic patamed, tients are associated with irritant contact dermatitis from common shampoo products
El5 SPECIFIC BINDING OF TMH MONOCLONAL ANTIBODIES TO THE b-LOCUS PKOTEIN, NOT TO THE AUTHENTIC TYROSINASE ENCODED AT THE c-LOCUS. Y. TOMITA, J. MATSUNAGA. & H. TAGAMI. Department of Dermatolwv. Tohoku Umversitv School of Medicme. Sendai TMH hybridomas were previously reported by Tomita et al. to produce monoclonal antibodies against murine and human T4tyrosinase (J Invest Dermatol 85:4X. 1985). However, TMH antibodies were unable to react with K1735 cells transfected with the authentic tyrosinase-cDNA construct but did react with those transfected with the pMT4-cDNA construct. The cDNA pMT4 was initially cloned as a putative tyrosinase cDNA by Shibahara et al. (Nucl Acld Res 14:2413, 1986), but it is now known to encode mouse brown (b) locus protein named “tyrosinase-related protein” by Jackson. TMH antibodies also recogmze hair bulbs of C~~BL/~J-@‘J/C?J mouse (B/B, c/c) lacking tyrosinase activity. but do not recoanize hair bulbs of b-locus DBAL? mutated m&se these
(b/b, c/C) observatmns,
recognize
which have authentic we conclude that
the protein
encoded
tyrosmase.
Considering
TMH antibodies at b-locus.
specifically
El8
El7 Subcellular Distribution Of Catechol-0.Methyltransferase And Melanotic Malignant Melanoma TAKAKAZU MISHIMA.
a-SMOOTH MUSCLE ACTIN EXPRESSION CELL EPI’IUELIOMA (BCE)
In Amelanotic
IN STROMA OF BASAL
TSUKAMOTO, WTAKA MWLlMA Department of Dermatology, Kobe University School of Medicine, Kobc, Japan
HIDEKAZU
SHIBATA, STAN PAVEL,MASAMITSU ICHIHASHI ANDYUTAKA Department of Dermatology, Kobe Univ. School of Medicine, Kobe
During melanogenes~s, not all indolic and phsnollc compounds incorporate 1nt0 the melanin polymer. Molecuiss which escape from their place of origin due to their easy oxidability to reactive quinones. may represent a threat to pigment cells O-methvlation catalvzed bv catechol.0.methvltransferase(COMT) prwents this oxidation and polymenratlon. Thus COMT is thought a protective mechanism in melanccytes and may even play a pan in the control of melanin formation. We studied subcellular localization of COMT in transplanted melanotic and amelanotlc hamster melanoma. Results show that COMT appears to be a cytoplasmic enzyme partly integrated with microsomes. Subcellular fractions obtained from ametanotic melanoma have been found to possess higher COMT activity than those from the pigmented tumor. The relatively low spwfic activity of COMT in coated vesicle fractions does not support 10sinhibitory function m melanin polymerization within these structures. However, COMT piefeient~atly located in cytosol and cytosolic membrane network cwtd save a detoxification role I” melanocytes.
is a major component of cytoskeletal proteins. B- and y- actin are expressed in all eukaryotic cells. We previously examined the altered expression of a-smooth muscle actin (a-Sm) in human pigment cell tumors by immunohistochemical analysis using anti-a-Sm monoclonal antibody (MoAb). This revealed a uniquely intense expression of a-&n in stroma surrounding melanoma cell nests, which was not seen in benign pigment cell tumors such as nexus cell nest. In this study, we examined immunohistochemically the expression of a-Sm in BCE which was often involved in desmoplastic response. At high frequency, anti-c&n MoAb positive myoiibroblasts were detected in desmoplasia surrounding BCE nests. Additionally, some tumor cells within a few cases showed anti-&m MoAb positive staining. It is suggested that desmoplasia in BCE might be caused by paracrine secretion of tumor cells. Actin usually
,
228